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Using deeply trapped intermediates to map the cytochrome c folding landscapeMutagenesis of histidine 26 demonstrates the importance of loop-loop and loop-protein interactions for the function of iso-1-cytochrome cRefolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force.Antibody-detected folding: kinetics of surface epitope formation are distinct from other folding phases.Cytochrome c folds through a smooth funnelCharacterization of equilibrium intermediates in denaturant-induced unfolding of ferrous and ferric cytochromes c using magnetic circular dichroism, circular dichroism, and optical absorption spectroscopies.Equilibrium unfolding of a small low-potential cytochrome, cytochrome c553 from Desulfovibrio vulgaris.
P2860
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P2860
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
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1997年學術文章
@zh-hant
name
Fast folding of cytochrome c
@ast
Fast folding of cytochrome c
@en
type
label
Fast folding of cytochrome c
@ast
Fast folding of cytochrome c
@en
prefLabel
Fast folding of cytochrome c
@ast
Fast folding of cytochrome c
@en
P2860
P356
P1433
P1476
Fast folding of cytochrome c
@en
P2093
P2860
P304
P356
10.1002/PRO.5560060311
P577
1997-03-01T00:00:00Z